Liam A Wilson, Jamie N Melville, Marcelo M Pedroso, Stefan Krco, Robert Hoelzle, Julian Zaugg, Gordon Southam, Bernardino Virdis, Paul Evans, Jenna Supper, Jeffrey R Harmer, Gene Tyson, Alice Clark, Gerhard Schenk, Paul V Bernhardt
Motivated by the ambition to establish an enzyme-driven bioleaching pathway for copper extraction, properties of the Type-1 copper protein rusticyanin from Acidithiobacillus ferrooxidans (AfR) were compared with those from an ancestral form of this enzyme (N0) and an archaeal enzyme identified in Ferroplasma acidiphilum (FaR). While both N0 and FaR show redox potentials similar to that of AfR their electron transport rates were significantly slower. The lack of a correlation between the redox potentials and electron transfer rates indicates that AfR and its associated electron transfer chain evolved to specifically facilitate the efficient conversion of the energy of iron oxidation to ATP formation...
March 25, 2024: Journal of Inorganic Biochemistry